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- W1993173602 abstract "Uteroglobin (UTG) forms a fascinating homodimeric structure that binds small- to medium-sized ligands through an internal hydrophobic cavity, located at the interface between the two monomers. Previous studies have shown that UTG fold is not limited to the UTG/CC10 family, whose sequence/structure relationships are highlighted here, but can be extended to the cap domain of Xanthobacter autotrophicus haloalkane dehalogenase. We show here that UTG fold is adopted by several other cap domains within the alpha/beta hydrolase family, making it a well-suited geode structure allowing it to sequester various hydrophobic molecules. Additionally, some data about a new crystal form of oxidized rabbit UTG are presented, completing previous structural studies, as well as results from molecular dynamics, suggesting an alternative way for the ligand to reach the internal cavity." @default.
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- W1993173602 date "2000-12-01" @default.
- W1993173602 modified "2023-10-03" @default.
- W1993173602 title "The Uteroglobin Fold" @default.
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- W1993173602 doi "https://doi.org/10.1111/j.1749-6632.2000.tb05522.x" @default.
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